Thermostability of reovirus disassembly intermediates (ISVPS) correlates with genetic, biochemical, and thermodynamic properties of major surface protein μ1

Jason K. Middleton, Tonya F. Severson, Kartik Chandran, Anne Lynn Gillian, John Yin, Max L. Nibert

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

Kinetic analyses of infectivity loss during thermal inactivation of reovirus particles revealed substantial differences between virions and infectious subvirion particles (ISVPs), as well as between the ISVPs of reoviruses type 1 Lang (T1L) and type 3 Dearing (T3D). The difference in thermal inactivation of T1L and T3D ISVPs was attributed to the major surface protein μ1 by genetic analyses with reassortant viruses and recoated cores. Irreversible conformational changes in ISVP-bound μ1 were shown to accompany thermal inactivation. The thermal inactivation of ISVPs approximated first-order kinetics over a range of temperatures, permitting the use of Arrhenius plots to estimate activation enthalpies and entropies that account for the different behaviors of T1L and T3D. An effect similar to enthalpy-entropy compensation was additionally noted for the ISVPs of these two isolates. Kinetic analyses with other ISVP-like particles, including ISVPs of a previously reported thermostable mutant, provided further insights into the role of μ1 as a determinant of thermostability. Intact virions, which contain σ3 bound to μ1 as their major surface proteins, exhibited greater thermostability than ISVPs and underwent thermal inactivation with kinetics that deviated from first order, suggesting a role for σ3 in both these properties. The distinct inactivation behaviors of ISVPs are consistent with their role as an essential intermediate in reovirus entry.

Original languageEnglish (US)
Pages (from-to)1051-1061
Number of pages11
JournalJournal of Virology
Volume76
Issue number3
StatePublished - 2002
Externally publishedYes

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Reoviridae
surface proteins
thermal stability
Thermodynamics
molecular genetics
thermodynamics
Molecular Biology
Membrane Proteins
Hot Temperature
heat inactivation
Entropy
Virion
Mammalian Orthoreovirus
Reassortant Viruses
kinetics
enthalpy
entropy
virion
Temperature
inactivation

ASJC Scopus subject areas

  • Immunology

Cite this

Thermostability of reovirus disassembly intermediates (ISVPS) correlates with genetic, biochemical, and thermodynamic properties of major surface protein μ1. / Middleton, Jason K.; Severson, Tonya F.; Chandran, Kartik; Gillian, Anne Lynn; Yin, John; Nibert, Max L.

In: Journal of Virology, Vol. 76, No. 3, 2002, p. 1051-1061.

Research output: Contribution to journalArticle

Middleton, Jason K. ; Severson, Tonya F. ; Chandran, Kartik ; Gillian, Anne Lynn ; Yin, John ; Nibert, Max L. / Thermostability of reovirus disassembly intermediates (ISVPS) correlates with genetic, biochemical, and thermodynamic properties of major surface protein μ1. In: Journal of Virology. 2002 ; Vol. 76, No. 3. pp. 1051-1061.
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